ID G7E6E4_MIXOS Unreviewed; 1180 AA.
AC G7E6E4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0008006|Google:ProtNLM};
GN Name=Mo05090 {ECO:0000313|EMBL:GAA98404.1};
GN ORFNames=E5Q_05090 {ECO:0000313|EMBL:GAA98404.1};
OS Mixia osmundae (strain CBS 9802 / IAM 14324 / JCM 22182 / KY 12970).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; Mixiomycetes;
OC Mixiales; Mixiaceae; Mixia.
OX NCBI_TaxID=764103 {ECO:0000313|EMBL:GAA98404.1, ECO:0000313|Proteomes:UP000009131};
RN [1] {ECO:0000313|Proteomes:UP000009131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 9802 / IAM 14324 / JCM 22182 / KY 12970
RC {ECO:0000313|Proteomes:UP000009131};
RX PubMed=21478649; DOI=10.2323/jgam.57.63;
RA Nishida H., Nagatsuka Y., Sugiyama J.;
RT "Draft genome sequencing of the enigmatic basidiomycete Mixia osmundae.";
RL J. Gen. Appl. Microbiol. 57:63-67(2011).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAA98404.1}.
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DR EMBL; BABT02000152; GAA98404.1; -; Genomic_DNA.
DR RefSeq; XP_014568993.1; XM_014713507.1.
DR AlphaFoldDB; G7E6E4; -.
DR STRING; 764103.G7E6E4; -.
DR GeneID; 26264862; -.
DR eggNOG; KOG1092; Eukaryota.
DR eggNOG; KOG3872; Eukaryota.
DR HOGENOM; CLU_273112_0_0_1; -.
DR InParanoid; G7E6E4; -.
DR OrthoDB; 463769at2759; -.
DR Proteomes; UP000009131; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProt.
DR GO; GO:0051716; P:cellular response to stimulus; IEA:UniProt.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 1.10.472.80; Ypt/Rab-GAP domain of gyp1p, domain 3; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR000195; Rab-GAP-TBC_dom.
DR InterPro; IPR035969; Rab-GAP_TBC_sf.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR15067; E3 UBIQUITIN-PROTEIN LIGASE RNF8; 1.
DR PANTHER; PTHR15067:SF8; E3 UBIQUITIN-PROTEIN LIGASE RNF8; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR Pfam; PF17123; zf-RING_11; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR SUPFAM; SSF47923; Ypt/Rab-GAP domain of gyp1p; 2.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000009131};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 401..467
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT DOMAIN 560..604
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 871..1103
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000259|PROSITE:PS50086"
FT REGION 102..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1180 AA; 126567 MW; FF1DDA0E5A3AF4B5 CRC64;
MPLLTLPLVH KKSRRASAEH HAGSSAASSP LSLVRLRRLT SSASLLQVPS QRETSHSTSV
QLARQRHTSL NVLVDARPPV DHSARTQAIV NDDQAKYIMA TPTSSASASS TELPTRMSTS
AVATPSGMAA GPLAMQRTRS HSGAPAPPAS PPIPPGSPNS QGRFNLSLGT LMSRRSRGSA
VPPLSPGSVL PRMATRDEGV VSQDWLPGSP SQSGGDSPGT SARSGYGFPT LRRRNSRRQQ
TSSQGSAVGS NPPGRPSSPF TAGSVPSASP LQNFASRSRS SSQPPAPAPG LVSALNESTS
SVRASAPTGG LRTVISTLTR PTPARSPSSN LLASGVTGED MLMGTSELDR PALLAPANSV
SDAVEPAAST RYYIRLVPNI DSTRSLQFEP ITRQVSPALP VKIGRFTDRG TNDASYNPNL
DVHSRKIAFR SKVVSRGHAE IWCDGTGAFC IRDTKSSSGT FLNHIRLSGP GLESRAYPLR
DGDMLQLGVD YQGGTEEIYR CVKMRVELNR GWQRGANAYN VNALKQLRAL QAPAETHAVA
TGTTSAAAVS NVKSSGVTDC CICLYSVTVC QALFIAPCSH CFHFKCIRPL LVQHHPAFSC
PICRTFADLD ADVEVDDDIL GMMDVDGVVA TPSQERETEI LAMPSMPLER PPPLDMSRSA
GAAPSPVDVF VADADHAAVP ISGPDGSASS VMIVGRTSRP GSIREAQAPG LQMTTSSPQY
SPDGQTRRPI APLRSSSRPE HSVSSSGPRT PESLYENAIT HSVPPSPPAG EDAGDAMTDV
KTEESAQPPA GVLGALISAV TGFTGNIEAS SSTSDSSMSS QDALAPKDAA SSSQGRVAVS
LMSATVAEFS EVLNAEQYVD LAKLRSYARH GVPLEIRGEV WLYLLGVFDA DRTNDVTSIR
AKLAQYAAMD KDLSDHALVR RIRAEATRYY HRRFHTRDKL GRQSSTHART TPVLPRIAPP
QSVPVPALEP QGDQIDFETF VQVSEHVVAT FLNRSVHAGY YPGLVSIAGC LIQTLKTEAG
VYYAFEKVAN MLDGLFEVLA MPYRVSHFVM LLRTFLPELY STFEEEEVDV NEIATLWFSN
LLSKELQDTD DLMRLWDAYF SLDPSNGDLL DFHAFVCLAI LSTRKEDLEE LDQSEARSLL
LSLPSLDVER ILAEASSMRL TFVSLSRTDR QDEDTAVPYY
//
